Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

Structure and dynamics of semaglutide- and taspoglutide-bound GLP-1R-Gs complexes
Xin Zhang, Matthew J. Belousoff, Yi Liang, et al.
Cell Reports (2021) Vol. 36, Iss. 2, pp. 109374-109374
Open Access | Times Cited: 46

Showing 1-25 of 46 citing articles:

Structural insights into multiplexed pharmacological actions of tirzepatide and peptide 20 at the GIP, GLP-1 or glucagon receptors
Fenghui Zhao, Qingtong Zhou, Zhaotong Cong, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 95
Structural determinants of dual incretin receptor agonism by tirzepatide
Bingfa Sun, Francis S. Willard, Dan Feng, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 13
Open Access | Times Cited: 68
GLP-1R signaling neighborhoods associate with the susceptibility to adverse drug reactions of incretin mimetics
Shane C. Wright, Aikaterini Motso, Stefania Koutsilieri, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 25
Discovery of Selenium-Containing Derivatives as Potent and Orally Bioavailable GLP-1R Agonists
Xuetao Chen, Shicheng Xu, Shuang Yang, et al.
Journal of Medicinal Chemistry (2025)
Closed Access | Times Cited: 1
Routine sub-2.5 Å cryo-EM structure determination of GPCRs
Radostin Danev, Matthew J. Belousoff, Yi-Lynn Liang, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 51
New Insights into the Structure and Function of Class B1 GPCRs
Brian P. Cary, Xin Zhang, Jianjun Cao, et al.
Endocrine Reviews (2022) Vol. 44, Iss. 3, pp. 492-517
Open Access | Times Cited: 37
Membranes under the Magnetic Lens: A Dive into the Diverse World of Membrane Protein Structures Using Cryo-EM
Sarah Piper, Rachel M. Johnson, Denise Wootten, et al.
Chemical Reviews (2022) Vol. 122, Iss. 17, pp. 13989-14017
Open Access | Times Cited: 33
Biased agonism and polymorphic variation at the GLP-1 receptor: Implications for the development of personalised therapeutics
Liliane El Eid, Christopher A. Reynolds, Alejandra Tomás, et al.
Pharmacological Research (2022) Vol. 184, pp. 106411-106411
Open Access | Times Cited: 29
A comprehensive guide for secondary structure and tertiary structure determination in peptides and proteins by circular dichroism spectrometer
Akhilesh Kumar Kuril, Ankur Vashi, Praveen Kumar Subbappa
Journal of Peptide Science (2024) Vol. 31, Iss. 1
Closed Access | Times Cited: 6
Structural Understanding of Peptide-Bound G Protein-Coupled Receptors: Peptide–Target Interactions
Yuxin Shi, Yi Chen, Liping Deng, et al.
Journal of Medicinal Chemistry (2023) Vol. 66, Iss. 2, pp. 1083-1111
Closed Access | Times Cited: 12
A Review on Forced Degradation Strategies to Establish the Stability of Therapeutic Peptide Formulations
Shikha Patel, Vivek K. Vyas, Priti Mehta
International Journal of Peptide Research and Therapeutics (2023) Vol. 29, Iss. 2
Closed Access | Times Cited: 12
Conformational Dynamics of the Activated GLP-1 Receptor-Gs Complex Revealed by Cross-Linking Mass Spectrometry and Integrative Structure Modeling
Shijia Yuan, Lisha Xia, Chenxi Wang, et al.
ACS Central Science (2023) Vol. 9, Iss. 5, pp. 992-1007
Open Access | Times Cited: 12
Structural analysis of the dual agonism at GLP-1R and GCGR
Yang Li, Qingtong Zhou, Antao Dai, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 33
Open Access | Times Cited: 12
Molecular insights into peptide agonist engagement with the PTH receptor
Brian P. Cary, Elliot Gerrard, Matthew J. Belousoff, et al.
Structure (2023) Vol. 31, Iss. 6, pp. 668-676.e5
Open Access | Times Cited: 11
Prolonged signaling of backbone-modified glucagon‐like peptide‐ 1 analogues with diverse receptor trafficking
Brian P. Cary, Marlies V. Hager, Zamara Mariam, et al.
Proceedings of the National Academy of Sciences (2025) Vol. 122, Iss. 14
Open Access
Structural pharmacology and mechanisms of GLP-1R signaling
Qingtong Zhou, Fenghui Zhao, Y Zhang, et al.
Trends in Pharmacological Sciences (2025)
Closed Access
Structural Biophysics-Guided Computational Design of Semaglutide Analogues to Enhance GLP-1R Activation
Wei Li
(2025)
Closed Access
Cryo-EM structure of the dual incretin receptor agonist, peptide-19, in complex with the glucagon-like peptide-1 receptor
Rachel M. Johnson, Xin Zhang, Sarah Piper, et al.
Biochemical and Biophysical Research Communications (2021) Vol. 578, pp. 84-90
Open Access | Times Cited: 27
Structure and Molecular Mechanism of Signaling for the Glucagon-like Peptide-1 Receptor Bound to Gs Protein and Exendin-P5 Biased Agonist
Bo Li, Krystyna Maruszko, Soo‐Kyung Kim, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 37, pp. 20422-20431
Open Access | Times Cited: 8
Implications of ligand-receptor binding kinetics on GLP-1R signalling
Peishen Zhao, Tin T. Truong, Jon Merlin, et al.
Biochemical Pharmacology (2022) Vol. 199, pp. 114985-114985
Closed Access | Times Cited: 13
New Long-Acting [89Zr]Zr-DFO GLP-1 PET Tracers with Increased Molar Activity and Reduced Kidney Accumulation
Jonas Wilbs, René Raavé, Milou Boswinkel, et al.
Journal of Medicinal Chemistry (2023) Vol. 66, Iss. 12, pp. 7772-7784
Open Access | Times Cited: 7
Differential Responses of the GLP-1 and GLP-2 Receptors to N-Terminal Modification of a Dual Agonist
Ruslan Gibadullin, Brian P. Cary, Samuel H. Gellman
Journal of the American Chemical Society (2023) Vol. 145, Iss. 22, pp. 12105-12114
Open Access | Times Cited: 7
In Silico Ligand Docking Approaches to Characterise the Binding of Known Allosteric Modulators to the Glucagon-Like Peptide 1 Receptor and Prediction of ADME/Tox Properties
Chiemela S. Odoemelam, Elena Hunter, John Simms, et al.
Applied Biosciences (2022) Vol. 1, Iss. 2, pp. 143-162
Open Access | Times Cited: 11
Understanding VPAC receptor family peptide binding and selectivity
Sarah Piper, Giuseppe Deganutti, Jessica Bo Li Lu, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 11
Partial agonism improves the anti-hyperglycaemic efficacy of an oxyntomodulin-derived GLP-1R/GCGR co-agonist
Philip Pickford, Maria Lucey, Roxana‐Maria Rujan, et al.
Molecular Metabolism (2021) Vol. 51, pp. 101242-101242
Open Access | Times Cited: 14
Page 1 - Next Page

Scroll to top